Header list of 1nla.pdb file
Complete list - t 27 2 Bytes
HEADER TRANSCRIPTION 06-JAN-03 1NLA
TITLE SOLUTION STRUCTURE OF SWITCH ARC, A MUTANT WITH 3(10) HELICES
TITLE 2 REPLACING A WILD-TYPE BETA-RIBBON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REPRESSOR ARC;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE P22;
SOURCE 3 ORGANISM_TAXID: 10754;
SOURCE 4 GENE: ARC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET800
KEYWDS 3(10) HELIX, BETA-RIBBON, BETA-SHEET, STRUCTURAL SWITCHING,
KEYWDS 2 TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 13
AUTHOR M.H.CORDES,N.P.WALSH,C.J.MCKNIGHT,R.T.SAUER
REVDAT 3 27-OCT-21 1NLA 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1NLA 1 VERSN
REVDAT 1 18-MAR-03 1NLA 0
JRNL AUTH M.H.CORDES,N.P.WALSH,C.J.MCKNIGHT,R.T.SAUER
JRNL TITL SOLUTION STRUCTURE OF SWITCH ARC, A MUTANT WITH 3(10)
JRNL TITL 2 HELICES REPLACING A WILD-TYPE BETA-RIBBON
JRNL REF J.MOL.BIOL. V. 326 899 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12581649
JRNL DOI 10.1016/S0022-2836(02)01425-0
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: EXPERIMENTALLY DERIVED RESTRAINTS
REMARK 3 INCLUDED 810 NOE DISTANCE RESTRAINTS PER MONOMER, ALONG WITH 3
REMARK 3 HYDROGEN BOND RESTRAINTS, 31 PHI-ANGLE RESTRAINTS AND 3 CHI1-
REMARK 3 ANGLE RESTRAINTS, FOR A TOTAL OF 847 RESTRAINTS PER MONOMER
REMARK 3 SPANNING RESIDUES 5-53. STRUCTURE CALCULATIONS WERE PERFORMED
REMARK 3 USING A SIMULATED ANNEALING PROTOCOL DESIGNED FOR SYMMETRIC
REMARK 3 DIMERS (M. NILGES, PROTEINS STRUCT. FUNCT. GEN, 17, 297 (1993)).
REMARK 3 AS STARTING POINTS FOR THE CALCULATION, 28 STRUCTURES WERE
REMARK 3 GENERATED IN WHICH THE CONFORMATION OF THE N-TERMINAL REGION
REMARK 3 (RESIDUES 1-13) WAS RANDOM, AND THAT OF THE REMAINDER OF THE
REMARK 3 PROTEIN RESTRAINED TO BE SIMILAR TO WILD-TYPE ARC. THE USE OF
REMARK 3 COMPLETELY RANDOM STARTING STRUCTURES LED TO EXTREMELY POOR
REMARK 3 CONVERGENCE RATES, BUT THOSE CALCULATIONS WHICH DID CONVERGE
REMARK 3 YIELDED STRUCTURES SIMILAR TO THOSE OBTAINED FROM CALCULATIONS
REMARK 3 USING NON-RANDOM STARTING STRUCTURES. EACH SEMI-RANDOM STARTING
REMARK 3 STRUCTURE WAS THEN ANNEALED TO A MODEL STRUCTURE USING THE
REMARK 3 DISTANCE, ANGLE AND HYDROGEN BOND RESTRAINTS MENTIONED ABOVE.
REMARK 3 TWO "SEED" RESTRAINTS, ARG 40 HE-PHE 45 HD AND TRP 14 HE3-TYR 38
REMARK 3 HE, WERE DESCRIBED AS UNAMBIGUOUSLY INTERMOLECULAR. IN THE WILD-
REMARK 3 TYPE ARC STRUCTURE, THE DIFFERENCE BETWEEN THE INTRA AND
REMARK 3 INTERMOLECULAR DISTANCES FOR THESE ATOMS IS >10 A. USE OF THE
REMARK 3 SEED RESTRAINTS IMPROVED CONVERGENCE BUT AGAIN DID NOT ALTER THE
REMARK 3 QUALITATIVE NATURE OF THE RESULTS. ALL OTHER NOE DISTANCE
REMARK 3 RESTRAINTS WERE DESCRIBED AMBIGUOUSLY USING SUM POTENTIALS.
REMARK 3 HYDROGEN-BOND RESTRAINTS IN ALPHA-HELICES WERE DESCRIBED AS
REMARK 3 INTRAMONOMER. IN THE CONFORMATIONAL SEARCH PHASE OF THE
REMARK 3 CALCULATIONS, NON-BONDED INTERACTIONS WERE COMPUTED ONLY BETWEEN
REMARK 3 C-ALPHA ATOMS WITH A VAN DER WAALS TERM OF 0.1. 13 OF 28
REMARK 3 CALCULATED STRUCTURES WERE ACCEPTED WITH NO ANGLE VIOLATIONS >5
REMARK 3 DEGREES AND NO MORE THAN TWO NOE VIOLATIONS >0.35 A. THESE
REMARK 3 COMPRISE THE ENSEMBLE SUBMITTED HERE.
REMARK 4
REMARK 4 1NLA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000017975.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303; 303
REMARK 210 PH : 4.8; 4.8; 4.67
REMARK 210 IONIC STRENGTH : 20MM PHOSPHATE; 20 MM PHOSPHATE;
REMARK 210 20 MM PHOSPHATE, 150 MM KCL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 4 MM UNIFORM 15N-LABELLED ARC
REMARK 210 REPRESSOR NL11/LN12 (SWITCH ARC);
REMARK 210 7.5 MM 10% 13C-LABELLED ARC
REMARK 210 REPRESSOR NL11/LN12 (SWITCH ARC);
REMARK 210 5 MM UNIFORM 15N-LABELLED ARC
REMARK 210 REPRESSOR NL11/LN12 (SWITCH ARC)
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; HNHB;
REMARK 210 HSQCS (HYDROGEN EXCHANGE)
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.1, NMRDRAW 2.1,
REMARK 210 NMRVIEW 3.1, X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 28
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 13
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-13
REMARK 465 RES C SSSEQI
REMARK 465 HIS A 54
REMARK 465 HIS A 55
REMARK 465 HIS A 56
REMARK 465 HIS A 57
REMARK 465 HIS A 58
REMARK 465 HIS A 59
REMARK 465 LYS A 60
REMARK 465 ASN A 61
REMARK 465 GLN A 62
REMARK 465 HIS A 63
REMARK 465 GLU A 64
REMARK 465 HIS B 54
REMARK 465 HIS B 55
REMARK 465 HIS B 56
REMARK 465 HIS B 57
REMARK 465 HIS B 58
REMARK 465 HIS B 59
REMARK 465 LYS B 60
REMARK 465 ASN B 61
REMARK 465 GLN B 62
REMARK 465 HIS B 63
REMARK 465 GLU B 64
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 2 MET A 4 -89.76 55.42
REMARK 500 2 ARG A 31 -162.91 -174.73
REMARK 500 2 MET B 4 -89.67 55.10
REMARK 500 2 ARG B 31 -163.27 -175.01
REMARK 500 3 LYS A 2 94.44 53.06
REMARK 500 3 SER A 5 -179.30 -62.76
REMARK 500 3 LYS A 6 -162.35 -73.67
REMARK 500 3 ARG A 31 -155.18 -133.44
REMARK 500 3 LYS B 2 94.66 52.96
REMARK 500 3 SER B 5 -179.22 -62.82
REMARK 500 3 LYS B 6 -162.14 -73.66
REMARK 500 3 ARG B 31 -155.69 -133.53
REMARK 500 4 SER A 5 -179.39 -69.38
REMARK 500 4 LEU A 11 31.65 -98.52
REMARK 500 4 ARG A 31 -162.84 -116.53
REMARK 500 4 SER B 5 -179.19 -69.46
REMARK 500 4 LEU B 11 31.62 -98.37
REMARK 500 4 ARG B 31 -162.64 -116.65
REMARK 500 5 LYS A 2 71.81 -171.69
REMARK 500 5 SER A 5 179.69 53.19
REMARK 500 5 MET A 7 162.26 57.87
REMARK 500 5 ARG A 31 -156.53 -114.15
REMARK 500 5 ILE A 51 -167.90 -104.93
REMARK 500 5 LYS B 2 72.20 -171.53
REMARK 500 5 SER B 5 179.66 53.05
REMARK 500 5 MET B 7 162.52 57.69
REMARK 500 5 ARG B 31 -156.88 -114.39
REMARK 500 5 ILE B 51 -168.27 -104.63
REMARK 500 6 LYS A 6 69.52 -156.65
REMARK 500 6 ARG A 31 -158.97 -131.73
REMARK 500 6 LYS B 6 69.52 -156.58
REMARK 500 6 ARG B 31 -159.06 -132.09
REMARK 500 7 LYS A 2 131.02 -172.53
REMARK 500 7 MET A 4 -157.96 54.28
REMARK 500 7 LYS A 6 -163.07 -68.69
REMARK 500 7 ARG A 31 -164.58 -121.17
REMARK 500 7 LYS B 2 130.95 -172.67
REMARK 500 7 MET B 4 -158.16 54.17
REMARK 500 7 LYS B 6 -162.92 -68.83
REMARK 500 7 ARG B 31 -164.57 -121.20
REMARK 500 8 ARG A 31 -154.89 -141.50
REMARK 500 8 ILE A 51 -63.51 -90.83
REMARK 500 8 ARG B 31 -154.88 -141.53
REMARK 500 8 ILE B 51 -63.21 -90.97
REMARK 500 9 LYS A 2 47.12 -101.12
REMARK 500 9 MET A 4 -59.77 -126.49
REMARK 500 9 SER A 5 23.88 -150.16
REMARK 500 9 LEU A 11 30.21 -93.77
REMARK 500 9 ILE A 51 -169.16 -128.19
REMARK 500 9 LYS B 2 47.15 -100.97
REMARK 500
REMARK 500 THIS ENTRY HAS 72 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 13 0.26 SIDE CHAIN
REMARK 500 1 ARG A 16 0.28 SIDE CHAIN
REMARK 500 1 ARG A 23 0.28 SIDE CHAIN
REMARK 500 1 ARG A 31 0.31 SIDE CHAIN
REMARK 500 1 ARG A 40 0.21 SIDE CHAIN
REMARK 500 1 ARG A 50 0.25 SIDE CHAIN
REMARK 500 1 ARG B 13 0.26 SIDE CHAIN
REMARK 500 1 ARG B 16 0.28 SIDE CHAIN
REMARK 500 1 ARG B 23 0.28 SIDE CHAIN
REMARK 500 1 ARG B 31 0.31 SIDE CHAIN
REMARK 500 1 ARG B 40 0.21 SIDE CHAIN
REMARK 500 1 ARG B 50 0.25 SIDE CHAIN
REMARK 500 2 ARG A 13 0.22 SIDE CHAIN
REMARK 500 2 ARG A 16 0.21 SIDE CHAIN
REMARK 500 2 ARG A 23 0.25 SIDE CHAIN
REMARK 500 2 ARG A 31 0.24 SIDE CHAIN
REMARK 500 2 ARG A 40 0.29 SIDE CHAIN
REMARK 500 2 ARG A 50 0.19 SIDE CHAIN
REMARK 500 2 ARG B 13 0.22 SIDE CHAIN
REMARK 500 2 ARG B 16 0.21 SIDE CHAIN
REMARK 500 2 ARG B 23 0.25 SIDE CHAIN
REMARK 500 2 ARG B 31 0.24 SIDE CHAIN
REMARK 500 2 ARG B 40 0.29 SIDE CHAIN
REMARK 500 2 ARG B 50 0.19 SIDE CHAIN
REMARK 500 3 ARG A 13 0.24 SIDE CHAIN
REMARK 500 3 ARG A 16 0.21 SIDE CHAIN
REMARK 500 3 ARG A 23 0.32 SIDE CHAIN
REMARK 500 3 ARG A 31 0.32 SIDE CHAIN
REMARK 500 3 ARG A 40 0.31 SIDE CHAIN
REMARK 500 3 ARG A 50 0.26 SIDE CHAIN
REMARK 500 3 ARG B 13 0.24 SIDE CHAIN
REMARK 500 3 ARG B 16 0.20 SIDE CHAIN
REMARK 500 3 ARG B 23 0.32 SIDE CHAIN
REMARK 500 3 ARG B 31 0.32 SIDE CHAIN
REMARK 500 3 ARG B 40 0.31 SIDE CHAIN
REMARK 500 3 ARG B 50 0.26 SIDE CHAIN
REMARK 500 4 ARG A 13 0.23 SIDE CHAIN
REMARK 500 4 ARG A 16 0.31 SIDE CHAIN
REMARK 500 4 ARG A 23 0.20 SIDE CHAIN
REMARK 500 4 ARG A 31 0.32 SIDE CHAIN
REMARK 500 4 ARG A 40 0.26 SIDE CHAIN
REMARK 500 4 ARG A 50 0.24 SIDE CHAIN
REMARK 500 4 ARG B 13 0.23 SIDE CHAIN
REMARK 500 4 ARG B 16 0.32 SIDE CHAIN
REMARK 500 4 ARG B 23 0.21 SIDE CHAIN
REMARK 500 4 ARG B 31 0.32 SIDE CHAIN
REMARK 500 4 ARG B 40 0.26 SIDE CHAIN
REMARK 500 4 ARG B 50 0.24 SIDE CHAIN
REMARK 500 5 ARG A 13 0.30 SIDE CHAIN
REMARK 500 5 ARG A 16 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 156 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QTG RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE SAME MUTANT
DBREF 1NLA A 1 53 UNP P03050 RARC_BPP22 1 53
DBREF 1NLA B 1 53 UNP P03050 RARC_BPP22 1 53
SEQADV 1NLA LEU A 11 UNP P03050 ASN 11 ENGINEERED MUTATION
SEQADV 1NLA ASN A 12 UNP P03050 LEU 12 ENGINEERED MUTATION
SEQADV 1NLA HIS A 54 UNP P03050 EXPRESSION TAG
SEQADV 1NLA HIS A 55 UNP P03050 EXPRESSION TAG
SEQADV 1NLA HIS A 56 UNP P03050 EXPRESSION TAG
SEQADV 1NLA HIS A 57 UNP P03050 EXPRESSION TAG
SEQADV 1NLA HIS A 58 UNP P03050 EXPRESSION TAG
SEQADV 1NLA HIS A 59 UNP P03050 EXPRESSION TAG
SEQADV 1NLA LYS A 60 UNP P03050 EXPRESSION TAG
SEQADV 1NLA ASN A 61 UNP P03050 EXPRESSION TAG
SEQADV 1NLA GLN A 62 UNP P03050 EXPRESSION TAG
SEQADV 1NLA HIS A 63 UNP P03050 EXPRESSION TAG
SEQADV 1NLA GLU A 64 UNP P03050 EXPRESSION TAG
SEQADV 1NLA LEU B 11 UNP P03050 ASN 11 ENGINEERED MUTATION
SEQADV 1NLA ASN B 12 UNP P03050 LEU 12 ENGINEERED MUTATION
SEQADV 1NLA HIS B 54 UNP P03050 EXPRESSION TAG
SEQADV 1NLA HIS B 55 UNP P03050 EXPRESSION TAG
SEQADV 1NLA HIS B 56 UNP P03050 EXPRESSION TAG
SEQADV 1NLA HIS B 57 UNP P03050 EXPRESSION TAG
SEQADV 1NLA HIS B 58 UNP P03050 EXPRESSION TAG
SEQADV 1NLA HIS B 59 UNP P03050 EXPRESSION TAG
SEQADV 1NLA LYS B 60 UNP P03050 EXPRESSION TAG
SEQADV 1NLA ASN B 61 UNP P03050 EXPRESSION TAG
SEQADV 1NLA GLN B 62 UNP P03050 EXPRESSION TAG
SEQADV 1NLA HIS B 63 UNP P03050 EXPRESSION TAG
SEQADV 1NLA GLU B 64 UNP P03050 EXPRESSION TAG
SEQRES 1 A 64 MET LYS GLY MET SER LYS MET PRO GLN PHE LEU ASN ARG
SEQRES 2 A 64 TRP PRO ARG GLU VAL LEU ASP LEU VAL ARG LYS VAL ALA
SEQRES 3 A 64 GLU GLU ASN GLY ARG SER VAL ASN SER GLU ILE TYR GLN
SEQRES 4 A 64 ARG VAL MET GLU SER PHE LYS LYS GLU GLY ARG ILE GLY
SEQRES 5 A 64 ALA HIS HIS HIS HIS HIS HIS LYS ASN GLN HIS GLU
SEQRES 1 B 64 MET LYS GLY MET SER LYS MET PRO GLN PHE LEU ASN ARG
SEQRES 2 B 64 TRP PRO ARG GLU VAL LEU ASP LEU VAL ARG LYS VAL ALA
SEQRES 3 B 64 GLU GLU ASN GLY ARG SER VAL ASN SER GLU ILE TYR GLN
SEQRES 4 B 64 ARG VAL MET GLU SER PHE LYS LYS GLU GLY ARG ILE GLY
SEQRES 5 B 64 ALA HIS HIS HIS HIS HIS HIS LYS ASN GLN HIS GLU
HELIX 1 1 PRO A 8 ARG A 13 5 6
HELIX 2 2 PRO A 15 GLY A 30 1 16
HELIX 3 3 SER A 32 GLY A 49 1 18
HELIX 4 4 PRO B 8 ARG B 13 5 6
HELIX 5 5 PRO B 15 GLY B 30 1 16
HELIX 6 6 SER B 32 GLY B 49 1 18
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - t 27 2 Bytes